Expression of Heat Shock Protein 70 (Hsp-70) in Children’s Acute Lymphoblastic Leukemia

Abstract

Heat shock protein (Hsp) 70 is one of the most common Hsp proteins found in humans. Like other types of Hsp, Hsp-70 acts as a chaperone protein in the process of protein synthesis. Its important role in protein synthesis means that these proteins are supposed to be inside the cell and cannot be examined outside the cell. In its development, Hsp-70 turned out to be examined outside of cells due to an increase in Hsp-70 caused by stress on cells which were caused by environmental stress conditions (heat shock, cold shock, heavy metal, oxygen-free radicals), inflammatory and infectious processes, ischemia, tissue damage, aging, and oncogenesis. Cancer studies have found high expression of Hsp-70 in solid tumors and hematological malignancies including ALL. High expression of Hsp-70 is said to have adverse implications on the outcome of ALL and therefore Hsp-70 is auspicious as a therapeutic target in the pediatric treatment of ALL. This review aims to elucidate the role of Hsp-70 expression in pediatric ALL patients.